A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein.

@article{Konno2000APU,
  title={A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein.},
  author={Takashi Konno and Yuji O Kamatari and Nobuo Tanaka and Hironari Kamikubo and Christopher M. Dobson and Kuniaki Nagayama},
  journal={Biochemistry},
  year={2000},
  volume={39 14},
  pages={4182-90}
}
Pepsin, a gastric aspartic proteinase, is a zymogen-derived protein that undergoes irreversible alkaline denaturation at pH 6-7. Detailed knowledge of the structure of the alkaline-denatured state is an important step in understanding the mechanism of the formation of the active enzyme. An extensive analysis of the denatured state at pH 8.0 was performed using a variety of techniques including (1)H nuclear magnetic resonance spectroscopy and solution X-ray scattering. This analysis indicates… CONTINUE READING
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